Functional heterogeneity of Escherichia coli ribonucleic acid polymerase holoenzyme.

On zone sedimentation Escherichia coli RNA polymerase holoenzyme exhibits functional heterogeneity with respect to template preference, regulation by ppGpp, and affinity for fMet-tRNA. The template preference of a subpopulation of RNA polymerase molecules correlates with both its sedimentation position and its ability to respond to effectors of polymerase selectivity. Incubation of such functionally distinct populations of enzyme molecules at physiological temperatures results in functional and structural equivalence. We suggest that RNA polymerase normally exists as a mixture of interconvertible forms and that promoter selection can be controlled by varying the number and proportions of forms present.